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HEADER HYDROLASE 26-SEP-19 6SXP
TITLE STRUCTURE OF ESTER-HYDROLASE EH3 FROM THE METAGENOME OF MARINE
TITLE 2 SEDIMENTS AT MILAZZO HARBOR (SICILY, ITALY)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: UNCULTURED BACTERIUM;
SOURCE 3 ORGANISM_TAXID: 77133;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI MC1061;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 1211845;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PBXNH3
KEYWDS ESTER HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR I.CEA-RAMA,J.SANZ-APARICIO
REVDAT 1 20-JAN-21 6SXP 0
JRNL AUTH C.I.GIUNTA,I.CEA-RAMA,S.ALONSO,M.L.BRIAND,R.BARGIELA,
JRNL AUTH 2 C.COSCOLIN,P.F.CORVINI,M.FERRER,J.SANZ-APARICIO,
JRNL AUTH 3 P.SHAHGALDIAN
JRNL TITL TUNING THE PROPERTIES OF NATURAL PROMISCUOUS ENZYMES BY
JRNL TITL 2 ENGINEERING THEIR NANO-ENVIRONMENT.
JRNL REF ACS NANO 2020
JRNL REFN ESSN 1936-086X
JRNL PMID 33306346
JRNL DOI 10.1021/ACSNANO.0C08716
REMARK 2
REMARK 2 RESOLUTION. 2.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0238
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.72
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 34279
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.203
REMARK 3 R VALUE (WORKING SET) : 0.202
REMARK 3 FREE R VALUE : 0.228
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 1723
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.15
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.21
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2500
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.85
REMARK 3 BIN R VALUE (WORKING SET) : 0.2260
REMARK 3 BIN FREE R VALUE SET COUNT : 117
REMARK 3 BIN FREE R VALUE : 0.2570
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5109
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 20
REMARK 3 SOLVENT ATOMS : 310
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.03
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.96000
REMARK 3 B22 (A**2) : -1.48000
REMARK 3 B33 (A**2) : -1.33000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.04000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.291
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.199
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.153
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.926
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.937
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.917
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5229 ; 0.005 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 4797 ; 0.002 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7073 ; 1.388 ; 1.639
REMARK 3 BOND ANGLES OTHERS (DEGREES): 11179 ; 1.284 ; 1.575
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 673 ; 6.350 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 265 ;34.225 ;23.472
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 874 ;14.054 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 30 ;19.198 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 686 ; 0.066 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5938 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1020 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 1
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 9 347 B 9 347 11025 0.060 0.050
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 6SXP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-SEP-19.
REMARK 100 THE DEPOSITION ID IS D_1292104512.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JUL-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALBA
REMARK 200 BEAMLINE : XALOC
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.07218
REMARK 200 MONOCHROMATOR : SI(111) CHANNEL-CUT, CRYOCOOLED
REMARK 200 OPTICS : KB FOCUSING MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 1.11.1
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36003
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.150
REMARK 200 RESOLUTION RANGE LOW (A) : 45.760
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 5.500
REMARK 200 R MERGE (I) : 0.15000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.22
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.60
REMARK 200 R MERGE FOR SHELL (I) : 0.64800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP 11.5.02
REMARK 200 STARTING MODEL: 5HC0
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.67
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 24% PEG 3000, 0.2M MGCL2, 0.1M BIS
REMARK 280 -TRIS PH 6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 91.64800
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 25.80750
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 91.64800
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 25.80750
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2800 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24470 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 HIS A -9
REMARK 465 HIS A -8
REMARK 465 LEU A -7
REMARK 465 GLU A -6
REMARK 465 VAL A -5
REMARK 465 LEU A -4
REMARK 465 PHE A -3
REMARK 465 GLN A -2
REMARK 465 GLY A -1
REMARK 465 PRO A 0
REMARK 465 SER A 1
REMARK 465 PRO A 2
REMARK 465 ASP A 3
REMARK 465 THR A 4
REMARK 465 THR A 5
REMARK 465 SER A 6
REMARK 465 LEU A 7
REMARK 465 ASN A 8
REMARK 465 GLY A 348
REMARK 465 ALA A 349
REMARK 465 MET B -18
REMARK 465 HIS B -17
REMARK 465 HIS B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 HIS B -9
REMARK 465 HIS B -8
REMARK 465 LEU B -7
REMARK 465 GLU B -6
REMARK 465 VAL B -5
REMARK 465 LEU B -4
REMARK 465 PHE B -3
REMARK 465 GLN B -2
REMARK 465 GLY B -1
REMARK 465 PRO B 0
REMARK 465 SER B 1
REMARK 465 PRO B 2
REMARK 465 ASP B 3
REMARK 465 THR B 4
REMARK 465 THR B 5
REMARK 465 SER B 6
REMARK 465 LEU B 7
REMARK 465 ASN B 8
REMARK 465 ALA B 25
REMARK 465 PHE B 26
REMARK 465 PRO B 27
REMARK 465 MET B 28
REMARK 465 MET B 29
REMARK 465 ALA B 349
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 PRO A 27 -178.61 -65.72
REMARK 500 MET A 29 -136.81 54.70
REMARK 500 GLU A 30 -45.10 -130.73
REMARK 500 MET A 117 173.94 76.67
REMARK 500 ASP A 142 75.32 -104.42
REMARK 500 LEU A 147 -57.67 -123.89
REMARK 500 SER A 150 -155.45 -97.22
REMARK 500 SER A 192 -121.94 63.85
REMARK 500 CYS A 221 60.95 30.41
REMARK 500 PHE A 233 79.33 -117.83
REMARK 500 MET A 243 -49.27 74.10
REMARK 500 PRO A 310 95.05 -67.40
REMARK 500 HIS A 321 121.08 -38.86
REMARK 500 GLN B 31 118.85 -28.46
REMARK 500 MET B 117 173.70 76.69
REMARK 500 ASP B 142 74.71 -104.81
REMARK 500 LEU B 147 -57.27 -124.13
REMARK 500 SER B 150 -155.58 -96.77
REMARK 500 SER B 192 -123.32 65.13
REMARK 500 CYS B 221 62.40 29.62
REMARK 500 PHE B 233 79.02 -117.30
REMARK 500 MET B 243 -52.13 74.66
REMARK 500 PRO B 269 -19.58 -49.99
REMARK 500 PRO B 310 95.00 -67.78
REMARK 500 HIS B 321 120.84 -38.29
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 403
DBREF1 6SXP A 2 348 UNP A0A2K8JN75_9BACT
DBREF2 6SXP A A0A2K8JN75 2 348
DBREF1 6SXP B 2 348 UNP A0A2K8JN75_9BACT
DBREF2 6SXP B A0A2K8JN75 2 348
SEQADV 6SXP MET A -18 UNP A0A2K8JN7 INITIATING METHIONINE
SEQADV 6SXP HIS A -17 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SXP HIS A -16 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SXP HIS A -15 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SXP HIS A -14 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SXP HIS A -13 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SXP HIS A -12 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SXP HIS A -11 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SXP HIS A -10 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SXP HIS A -9 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SXP HIS A -8 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SXP LEU A -7 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SXP GLU A -6 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SXP VAL A -5 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SXP LEU A -4 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SXP PHE A -3 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SXP GLN A -2 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SXP GLY A -1 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SXP PRO A 0 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SXP SER A 1 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SXP ALA A 349 UNP A0A2K8JN7 INSERTION
SEQADV 6SXP MET B -18 UNP A0A2K8JN7 INITIATING METHIONINE
SEQADV 6SXP HIS B -17 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SXP HIS B -16 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SXP HIS B -15 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SXP HIS B -14 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SXP HIS B -13 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SXP HIS B -12 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SXP HIS B -11 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SXP HIS B -10 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SXP HIS B -9 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SXP HIS B -8 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SXP LEU B -7 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SXP GLU B -6 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SXP VAL B -5 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SXP LEU B -4 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SXP PHE B -3 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SXP GLN B -2 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SXP GLY B -1 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SXP PRO B 0 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SXP SER B 1 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SXP ALA B 349 UNP A0A2K8JN7 INSERTION
SEQRES 1 A 368 MET HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS LEU GLU
SEQRES 2 A 368 VAL LEU PHE GLN GLY PRO SER PRO ASP THR THR SER LEU
SEQRES 3 A 368 ASN ILE ALA ASP ASP VAL ARG MET ASP PRO ARG LEU LYS
SEQRES 4 A 368 ALA MET LEU ALA ALA PHE PRO MET MET GLU GLN GLN THR
SEQRES 5 A 368 PHE GLN THR ARG GLU GLU GLN VAL ALA ASN ALA ASN THR
SEQRES 6 A 368 PRO GLU ALA THR ALA ALA ARG GLU GLN LEU LYS MET MET
SEQRES 7 A 368 MET ASP MET MET ASP SER GLU GLU PHE ALA PRO SER ASP
SEQRES 8 A 368 ASN LEU ASP ILE SER THR ARG GLU PHE THR SER SER PRO
SEQRES 9 A 368 ASP GLY ASN ALA ILE LYS ILE GLN PHE ILE ARG PRO LYS
SEQRES 10 A 368 GLY LYS GLN LYS VAL PRO CYS VAL TYR TYR ILE HIS GLY
SEQRES 11 A 368 GLY GLY MET MET ILE MET SER ALA PHE TYR GLY ASN TYR
SEQRES 12 A 368 ARG ALA TRP GLY LYS MET ILE ALA ASN ASN GLY VAL ALA
SEQRES 13 A 368 VAL ALA MET VAL ASP PHE ARG ASN CYS LEU SER PRO SER
SEQRES 14 A 368 SER ALA PRO GLU VAL ALA PRO PHE PRO ALA GLY LEU ASN
SEQRES 15 A 368 ASP CYS VAL SER GLY LEU LYS TRP VAL SER GLU ASN ALA
SEQRES 16 A 368 ASP GLU LEU SER ILE ASP LYS ASN LYS ILE ILE ILE ALA
SEQRES 17 A 368 GLY GLU SER GLY GLY GLY ASN LEU THR LEU ALA THR GLY
SEQRES 18 A 368 LEU LYS LEU LYS GLN ASP GLY ASN ILE ASP LEU VAL LYS
SEQRES 19 A 368 GLY LEU TYR ALA LEU CYS PRO TYR ILE ALA GLY LYS TRP
SEQRES 20 A 368 PRO GLN ASP ARG PHE PRO SER SER SER GLU ASN ASN GLY
SEQRES 21 A 368 ILE MET ILE GLU LEU HIS ASN ASN GLN GLY ALA LEU ALA
SEQRES 22 A 368 TYR GLY ILE GLU GLN LEU GLU ALA GLU ASN PRO LEU ALA
SEQRES 23 A 368 TRP PRO SER PHE ALA SER ALA GLU ASP MET GLN GLY LEU
SEQRES 24 A 368 PRO PRO THR VAL ILE ASN VAL ASN GLU CYS ASP PRO LEU
SEQRES 25 A 368 ARG ASP GLU GLY ILE ASP PHE TYR ARG ARG LEU MET ALA
SEQRES 26 A 368 ALA GLY VAL PRO ALA ARG CYS ARG GLN VAL MET GLY THR
SEQRES 27 A 368 CYS HIS ALA GLY ASP MET PHE VAL ALA VAL ILE PRO ASP
SEQRES 28 A 368 VAL SER ALA ASP THR ALA ALA ASP ILE ALA ARG THR ALA
SEQRES 29 A 368 LYS GLY GLY ALA
SEQRES 1 B 368 MET HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS LEU GLU
SEQRES 2 B 368 VAL LEU PHE GLN GLY PRO SER PRO ASP THR THR SER LEU
SEQRES 3 B 368 ASN ILE ALA ASP ASP VAL ARG MET ASP PRO ARG LEU LYS
SEQRES 4 B 368 ALA MET LEU ALA ALA PHE PRO MET MET GLU GLN GLN THR
SEQRES 5 B 368 PHE GLN THR ARG GLU GLU GLN VAL ALA ASN ALA ASN THR
SEQRES 6 B 368 PRO GLU ALA THR ALA ALA ARG GLU GLN LEU LYS MET MET
SEQRES 7 B 368 MET ASP MET MET ASP SER GLU GLU PHE ALA PRO SER ASP
SEQRES 8 B 368 ASN LEU ASP ILE SER THR ARG GLU PHE THR SER SER PRO
SEQRES 9 B 368 ASP GLY ASN ALA ILE LYS ILE GLN PHE ILE ARG PRO LYS
SEQRES 10 B 368 GLY LYS GLN LYS VAL PRO CYS VAL TYR TYR ILE HIS GLY
SEQRES 11 B 368 GLY GLY MET MET ILE MET SER ALA PHE TYR GLY ASN TYR
SEQRES 12 B 368 ARG ALA TRP GLY LYS MET ILE ALA ASN ASN GLY VAL ALA
SEQRES 13 B 368 VAL ALA MET VAL ASP PHE ARG ASN CYS LEU SER PRO SER
SEQRES 14 B 368 SER ALA PRO GLU VAL ALA PRO PHE PRO ALA GLY LEU ASN
SEQRES 15 B 368 ASP CYS VAL SER GLY LEU LYS TRP VAL SER GLU ASN ALA
SEQRES 16 B 368 ASP GLU LEU SER ILE ASP LYS ASN LYS ILE ILE ILE ALA
SEQRES 17 B 368 GLY GLU SER GLY GLY GLY ASN LEU THR LEU ALA THR GLY
SEQRES 18 B 368 LEU LYS LEU LYS GLN ASP GLY ASN ILE ASP LEU VAL LYS
SEQRES 19 B 368 GLY LEU TYR ALA LEU CYS PRO TYR ILE ALA GLY LYS TRP
SEQRES 20 B 368 PRO GLN ASP ARG PHE PRO SER SER SER GLU ASN ASN GLY
SEQRES 21 B 368 ILE MET ILE GLU LEU HIS ASN ASN GLN GLY ALA LEU ALA
SEQRES 22 B 368 TYR GLY ILE GLU GLN LEU GLU ALA GLU ASN PRO LEU ALA
SEQRES 23 B 368 TRP PRO SER PHE ALA SER ALA GLU ASP MET GLN GLY LEU
SEQRES 24 B 368 PRO PRO THR VAL ILE ASN VAL ASN GLU CYS ASP PRO LEU
SEQRES 25 B 368 ARG ASP GLU GLY ILE ASP PHE TYR ARG ARG LEU MET ALA
SEQRES 26 B 368 ALA GLY VAL PRO ALA ARG CYS ARG GLN VAL MET GLY THR
SEQRES 27 B 368 CYS HIS ALA GLY ASP MET PHE VAL ALA VAL ILE PRO ASP
SEQRES 28 B 368 VAL SER ALA ASP THR ALA ALA ASP ILE ALA ARG THR ALA
SEQRES 29 B 368 LYS GLY GLY ALA
HET GOL B 401 6
HET PEG B 402 7
HET PEG B 403 7
HETNAM GOL GLYCEROL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 GOL C3 H8 O3
FORMUL 4 PEG 2(C4 H10 O3)
FORMUL 6 HOH *310(H2 O)
HELIX 1 AA1 ASP A 16 PHE A 26 1 11
HELIX 2 AA2 THR A 36 ALA A 44 1 9
HELIX 3 AA3 THR A 46 MET A 62 1 17
HELIX 4 AA4 TYR A 121 ASN A 133 1 13
HELIX 5 AA5 PRO A 159 ASN A 175 1 17
HELIX 6 AA6 ASN A 175 SER A 180 1 6
HELIX 7 AA7 SER A 192 ASP A 208 1 17
HELIX 8 AA8 ASN A 210 VAL A 214 5 5
HELIX 9 AA9 PRO A 234 ASN A 239 1 6
HELIX 10 AB1 ASN A 249 ALA A 262 1 14
HELIX 11 AB2 TRP A 268 ALA A 272 5 5
HELIX 12 AB3 SER A 273 GLN A 278 1 6
HELIX 13 AB4 LEU A 293 ALA A 307 1 15
HELIX 14 AB5 ALA A 322 PHE A 326 5 5
HELIX 15 AB6 ILE A 330 GLY A 347 1 18
HELIX 16 AB7 ASP B 16 LEU B 23 1 8
HELIX 17 AB8 THR B 36 ALA B 44 1 9
HELIX 18 AB9 THR B 46 MET B 62 1 17
HELIX 19 AC1 TYR B 121 ASN B 133 1 13
HELIX 20 AC2 PRO B 159 ASN B 175 1 17
HELIX 21 AC3 ASN B 175 SER B 180 1 6
HELIX 22 AC4 SER B 192 ASP B 208 1 17
HELIX 23 AC5 ASN B 210 VAL B 214 5 5
HELIX 24 AC6 PRO B 234 ASN B 239 1 6
HELIX 25 AC7 ASN B 249 ALA B 262 1 14
HELIX 26 AC8 TRP B 268 ALA B 272 5 5
HELIX 27 AC9 SER B 273 GLN B 278 1 6
HELIX 28 AD1 LEU B 293 ALA B 307 1 15
HELIX 29 AD2 ALA B 322 PHE B 326 5 5
HELIX 30 AD3 ILE B 330 GLY B 347 1 18
SHEET 1 AA116 LEU A 74 THR A 82 0
SHEET 2 AA116 ALA A 89 PRO A 97 -1 O PHE A 94 N SER A 77
SHEET 3 AA116 ALA A 137 ASP A 142 -1 O ASP A 142 N LYS A 91
SHEET 4 AA116 VAL A 103 ILE A 109 1 N PRO A 104 O ALA A 137
SHEET 5 AA116 ILE A 181 GLU A 191 1 O ILE A 187 N TYR A 107
SHEET 6 AA116 GLY A 216 LEU A 220 1 O LEU A 220 N GLY A 190
SHEET 7 AA116 THR A 283 ASN A 288 1 O VAL A 284 N ALA A 219
SHEET 8 AA116 ALA A 311 VAL A 316 1 O ARG A 314 N VAL A 287
SHEET 9 AA116 ALA B 311 VAL B 316 -1 O GLN B 315 N GLN A 315
SHEET 10 AA116 THR B 283 ASN B 288 1 N VAL B 287 O ARG B 314
SHEET 11 AA116 GLY B 216 LEU B 220 1 N ALA B 219 O VAL B 284
SHEET 12 AA116 ILE B 181 GLU B 191 1 N GLY B 190 O LEU B 220
SHEET 13 AA116 VAL B 103 ILE B 109 1 N TYR B 107 O ILE B 187
SHEET 14 AA116 ALA B 137 ASP B 142 1 O ALA B 137 N PRO B 104
SHEET 15 AA116 ALA B 89 PRO B 97 -1 N LYS B 91 O ASP B 142
SHEET 16 AA116 LEU B 74 THR B 82 -1 N SER B 77 O PHE B 94
CISPEP 1 SER A 84 PRO A 85 0 7.30
CISPEP 2 SER A 84 PRO A 85 0 8.43
CISPEP 3 PHE A 158 PRO A 159 0 2.44
CISPEP 4 TRP A 228 PRO A 229 0 -2.89
CISPEP 5 SER B 84 PRO B 85 0 9.22
CISPEP 6 PHE B 158 PRO B 159 0 2.61
CISPEP 7 TRP B 228 PRO B 229 0 -2.51
SITE 1 AC1 7 MET B 115 TYR B 223 TRP B 228 GLU B 245
SITE 2 AC1 7 LEU B 246 ASN B 248 GLY B 251
SITE 1 AC2 4 SER A 84 ASP B 208 GLY B 209 ASN B 210
SITE 1 AC3 6 ASP B 295 ILE B 298 ASP B 299 ARG B 302
SITE 2 AC3 6 HOH B 542 HOH B 595
CRYST1 183.296 51.615 70.254 90.00 93.86 90.00 C 1 2 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.005456 0.000000 0.000368 0.00000
SCALE2 0.000000 0.019374 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014266 0.00000
TER 2576 GLY A 347
TER 5114 GLY B 348
MASTER 366 0 3 30 16 0 5 6 5439 2 20 58
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